Inhibition of Membrane-Type Serine Protease 1/Matriptase by Natural and Synthetic Protease Inhibitors
نویسندگان
چکیده
منابع مشابه
The mechanism of inhibition of antibody-based inhibitors of membrane-type serine protease 1 (MT-SP1).
The mechanisms of inhibition of two novel scFv antibody inhibitors of the serine protease MT-SP1/matriptase reveal the basis of their potency and specificity. Kinetic experiments characterize the inhibitors as extremely potent inhibitors with K(I) values in the low picomolar range that compete with substrate binding in the S1 site. Alanine scanning of the loops surrounding the protease active s...
متن کاملGlycosaminoglycans: Synthetic fragments and their interaction with serine protease inhibitors
Glycosaminoglycans such as e.g. heparin, heparan sulphate and dermatan sulphate display a broad variety of biological activities. Unique, Well-defined domains in some glycosaminoglycans have been characterized that are responsible for the biological activity. For instance, a unique pentasaccharide domain in heparin could be identified which binds and activates the serine protease inhibitor (ser...
متن کاملPotent and selective inhibition of membrane-type serine protease 1 by human single-chain antibodies.
Specific human antibodies targeting proteases expressed on cancer cells can be valuable reagents for diagnosis, prognosis, and therapy of cancer. To this end, a phage-displayed antibody library was screened against a cancer-associated serine protease, MT-SP1. A protein inhibitor of serine proteases that binds to a defined surface of MT-SP1 was used in an affinity-based washing procedure. Six an...
متن کاملEngineering thermostability in serine protease inhibitors.
Unlike most globular proteins, the native form of serine protease inhibitors (serpins) is strained. Previous studies of human alpha(1)-antitrypsin, a prototype plasma serpin, revealed that various unfavorable interactions, such as overpacking of side chains, buried polar groups and cavities, are the structural basis of the strain. The local strain could be relieved by various stabilizing single...
متن کاملStructural energetics of serine protease inhibition*
We have investigated the binding of the serine protease inhibitor, turkey ovomucoid third domain (OMTKY3), to the serine protease, porcine pancreatic elastase (PPE), using isothermal titration calorimetry and structural energetics calculations. The calculations predict that the binding at 25 8C is characterized by a negligible DH 8, a large and positive DS 8, and a large and negative DCp, resul...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Nutritional Science and Vitaminology
سال: 2003
ISSN: 0301-4800,1881-7742
DOI: 10.3177/jnsv.49.27